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Database: UniProt
Entry: J3YT38_9ENTR
LinkDB: J3YT38_9ENTR
Original site: J3YT38_9ENTR 
ID   J3YT38_9ENTR            Unreviewed;       358 AA.
AC   J3YT38;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU366023};
DE            Short=FBP aldolase {ECO:0000256|RuleBase:RU366023};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU366023};
GN   ORFNames=A35E_00267 {ECO:0000313|EMBL:AFP85573.1};
OS   secondary endosymbiont of Heteropsylla cubana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts.
OX   NCBI_TaxID=134287 {ECO:0000313|EMBL:AFP85573.1, ECO:0000313|Proteomes:UP000003937};
RN   [1] {ECO:0000313|EMBL:AFP85573.1, ECO:0000313|Proteomes:UP000003937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hcub_S {ECO:0000313|EMBL:AFP85573.1};
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
CC   -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC       phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC       (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC       the reverse reaction in glycolysis. {ECO:0000256|RuleBase:RU366023}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000441,
CC         ECO:0000256|RuleBase:RU366023};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001359-3,
CC         ECO:0000256|RuleBase:RU366023};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC       provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3,
CC       ECO:0000256|RuleBase:RU366023};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU366023}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|ARBA:ARBA00005812, ECO:0000256|RuleBase:RU366023}.
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DR   EMBL; CP003547; AFP85573.1; -; Genomic_DNA.
DR   RefSeq; WP_014888870.1; NC_018420.1.
DR   AlphaFoldDB; J3YT38; -.
DR   STRING; 134287.A35E_00267; -.
DR   KEGG; sehc:A35E_00267; -.
DR   PATRIC; fig|134287.3.peg.258; -.
DR   HOGENOM; CLU_036923_0_0_6; -.
DR   OrthoDB; 9803995at2; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000003937; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00946; FBP_aldolase_IIA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006411; Fruct_bisP_bact.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01520; FruBisAldo_II_A; 1.
DR   PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU366023};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU366023};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001359-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003937};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT   ACT_SITE        109
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         227
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         265..267
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         286..289
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   358 AA;  39389 MW;  708B6E49B46D0ADA CRC64;
     MSKILDFLKP GVITGDDVQK VFKIARQNNF ALPAVNCIGT DSINSALEVA AKVRSPIIIQ
     FSNGGANFIA GKGIKSTNQT AAVLGGISGA LHVHHMAKYY NASVILHTDH CVKKNLSWID
     GLLDAGEKHY ARTGTTLFSS HMIDLSEEPL EQNIEISVKY LTRMVKLGMT LEVELGCTGG
     EEDGVDNSYL DKSTLYTKPE DVAYAYEKLS LISSNFIIAA AFGNVHGVYK KGNVELIPTI
     LDNSQKYVAK KFNLQEKPLN LVFHGGSGSS LKDIQEAIKC GVIKMNIDTD IQWATWKGIM
     EYYKMNESYM QAQIGNPEGA NKPNKQFYDP RAWIRAAQIS TITSLEQVFK TLNAVNLL
//
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